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Article

Active and inactive state structures of unliganded Lactobacillus casei allosteric L-lactate dehydrogenase.

Proteins - 15 Feb 2010

Arai Kazuhito, Ishimitsu Toshihiro, Fushinobu Shinya, Uchikoba Hiroyuki, Matsuzawa Hiroshi, Taguchi Hayao

Abstract excerpt

Lactobacillus casei L-lactate dehydrogenase (LCLDH) is activated through the homotropic and heterotropic activation effects of pyruvate and fructose 1,6-bisphosphate (FBP), respectively, and exhibits unusually high pH-dependence in the allosteric effects of these ligands. The active (R) and inactive (T) state structures of unliganded LCLDH were determined at 2.5 and 2.6 A resolution, respectively. In the...

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PMID: 19787773
DOI: 10.1002/prot.22597

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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